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- PDB-7pna: Evolved unspecific peroxygenase with A77L mutation in complex wit... -

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Basic information

Entry
Database: PDB / ID: 7pna
TitleEvolved unspecific peroxygenase with A77L mutation in complex with 12-methoxylauric acid
ComponentsAromatic peroxygenaseUnspecific peroxygenase
KeywordsOXIDOREDUCTASE / 12-methoxylauric acid complex / peroxygenase / peroxidase
Function / homology
Function and homology information


unspecific peroxygenase / hydrogen peroxide catabolic process / peroxidase activity / heme binding / metal ion binding
Similarity search - Function
Chloroperoxidase / Chloroperoxidase-like superfamily / Peroxidase, family 2 / Heme haloperoxidase family profile.
Similarity search - Domain/homology
12-methoxylauric acid / PROTOPORPHYRIN IX CONTAINING FE / PHOSPHATE ION / Aromatic peroxygenase
Similarity search - Component
Biological speciesAgrocybe aegerita (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.9 Å
AuthorsFernandez-Garcia, A. / Sanz-Aparicio, J.
Funding support Spain, 1items
OrganizationGrant numberCountry
Spanish Ministry of Science, Innovation, and UniversitiesComunidad de Madrid Synergy CAM project Y2018/BIO-4738-EVOCHIMERA-CM Spain
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2023
Title: Engineering a Highly Regioselective Fungal Peroxygenase for the Synthesis of Hydroxy Fatty Acids.
Authors: Gomez de Santos, P. / Gonzalez-Benjumea, A. / Fernandez-Garcia, A. / Aranda, C. / Wu, Y. / But, A. / Molina-Espeja, P. / Mate, D.M. / Gonzalez-Perez, D. / Zhang, W. / Kiebist, J. / ...Authors: Gomez de Santos, P. / Gonzalez-Benjumea, A. / Fernandez-Garcia, A. / Aranda, C. / Wu, Y. / But, A. / Molina-Espeja, P. / Mate, D.M. / Gonzalez-Perez, D. / Zhang, W. / Kiebist, J. / Scheibner, K. / Hofrichter, M. / Swiderek, K. / Moliner, V. / Sanz-Aparicio, J. / Hollmann, F. / Gutierrez, A. / Alcalde, M.
History
DepositionSep 6, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 25, 2023Provider: repository / Type: Initial release
Revision 1.1Feb 1, 2023Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Mar 1, 2023Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.year
Revision 1.3Feb 7, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Aromatic peroxygenase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,09811
Polymers35,9901
Non-polymers2,10810
Water2,396133
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: PISA
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3020 Å2
ΔGint-35 kcal/mol
Surface area13780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)51.466, 58.082, 61.198
Angle α, β, γ (deg.)90.000, 109.930, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein / Sugars , 2 types, 6 molecules A

#1: Protein Aromatic peroxygenase / Unspecific peroxygenase / AaP


Mass: 35990.012 Da / Num. of mol.: 1 / Mutation: V57A, L67F, V75I, A77L, I248V, F311L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Agrocybe aegerita (fungus) / Gene: APO1 / Production host: Komagataella phaffii CBS 7435 (fungus) / References: UniProt: B9W4V6, unspecific peroxygenase
#6: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 6 types, 138 molecules

#2: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#3: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#7: Chemical ChemComp-7UT / 12-methoxylauric acid / 12-methoxydodecanoic acid


Mass: 230.344 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C13H26O3 / Feature type: SUBJECT OF INVESTIGATION
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 133 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.34 Å3/Da / Density % sol: 47.41 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.6
Details: 1.6M sodium potassium phosphate pH 5.6, 5% MPD Soaking: 40 mM 12-metoxilauric acid, 30 minutes, cryoprotected with 25% glycerol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.97926 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jun 3, 2020 / Details: KB MIRRORS
RadiationMonochromator: M / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97926 Å / Relative weight: 1
ReflectionResolution: 1.9→48.43 Å / Num. obs: 26835 / % possible obs: 99.8 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.182 / Rpim(I) all: 0.077 / Rrim(I) all: 0.198 / Χ2: 0.94 / Net I/σ(I): 10.1
Reflection shellResolution: 1.9→1.94 Å / Redundancy: 6.7 % / Rmerge(I) obs: 0.68 / Mean I/σ(I) obs: 4.4 / Num. unique obs: 1687 / Rpim(I) all: 0.281 / Rrim(I) all: 0.737 / Χ2: 0.97 / % possible all: 99.4

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 5OXU

5oxu


Resolution: 1.9→48.43 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.937 / SU B: 2.691 / SU ML: 0.08 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.14 / ESU R Free: 0.125 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.1955 1203 4.5 %RANDOM
Rwork0.1637 ---
obs0.1651 25620 99.77 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 75.87 Å2 / Biso mean: 17.541 Å2 / Biso min: 8.79 Å2
Baniso -1Baniso -2Baniso -3
1--0.73 Å20 Å20.73 Å2
2---1.53 Å2-0 Å2
3---1.37 Å2
Refinement stepCycle: final / Resolution: 1.9→48.43 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2517 0 136 133 2786
Biso mean--24.17 24.18 -
Num. residues----325
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0132770
X-RAY DIFFRACTIONr_bond_other_d0.0010.0172489
X-RAY DIFFRACTIONr_angle_refined_deg1.4731.7263792
X-RAY DIFFRACTIONr_angle_other_deg1.4581.6415740
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.8045332
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.87521.961153
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.86715387
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.8461520
X-RAY DIFFRACTIONr_chiral_restr0.0750.2350
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.023221
X-RAY DIFFRACTIONr_gen_planes_other0.0080.02685
LS refinement shellResolution: 1.9→1.949 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.219 95 -
Rwork0.176 1841 -
all-1936 -
obs--99.38 %

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